SitesBLAST
Comparing WP_078716728.1 NCBI__GCF_900167125.1:WP_078716728.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 93% coverage: 16:387/400 of query aligns to 35:415/429 of P73133
- Y39 (= Y20) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S106) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G107) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A108) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R143) mutation to A: 4100-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 9.5% of N-acetylornithine aminotransferase wild-type activity.
- E223 (= E198) mutation to A: 65-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 50% of N-acetylornithine aminotransferase wild-type activity.; mutation to S: 73-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Shows 160% of N-acetylornithine aminotransferase wild-type activity.
- D251 (= D226) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q229) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K255) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T284) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R374) mutation to A: 2080-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 18% of N-acetylornithine aminotransferase wild-type activity.
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
42% identity, 96% coverage: 16:397/400 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F140), E179 (= E193), D212 (= D226), Q215 (= Q229), K241 (= K255), T270 (= T284), R352 (= R374)
- binding pyridoxal-5'-phosphate: G95 (= G107), T96 (≠ A108), F127 (= F140), H128 (= H141), E179 (= E193), D212 (= D226), V214 (= V228), K241 (= K255)
Q9M8M7 Acetylornithine aminotransferase, chloroplastic/mitochondrial; ACOAT; Acetylornithine transaminase; AOTA; Protein HOPW1-1-INTERACTING 1; EC 2.6.1.11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
41% identity, 100% coverage: 2:400/400 of query aligns to 55:456/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
42% identity, 96% coverage: 16:397/400 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- K242 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T284) binding pyridoxal 5'-phosphate
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
40% identity, 96% coverage: 16:400/400 of query aligns to 11:393/393 of 2ordA
- active site: F134 (= F140), E186 (= E193), D219 (= D226), Q222 (= Q229), K248 (= K255), T276 (= T284), R367 (= R374)
- binding pyridoxal-5'-phosphate: G102 (= G107), T103 (≠ A108), F134 (= F140), H135 (= H141), E186 (= E193), D219 (= D226), V221 (= V228), Q222 (= Q229), K248 (= K255)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
40% identity, 96% coverage: 16:400/400 of query aligns to 3:385/385 of Q9X2A5
- GT 94:95 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- T268 (= T284) binding pyridoxal 5'-phosphate
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
39% identity, 96% coverage: 4:386/400 of query aligns to 7:384/400 of 4addA
- active site: F136 (= F140), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R374)
- binding pyridoxal-5'-phosphate: G103 (= G107), A104 (= A108), F136 (= F140), H137 (= H141), D221 (= D226), V223 (= V228), K250 (= K255)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y20), F136 (= F140), R139 (= R143)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
39% identity, 96% coverage: 4:386/400 of query aligns to 7:384/401 of 4adbB
- active site: F136 (= F140), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R374)
- binding pyridoxal-5'-phosphate: S102 (= S106), G103 (= G107), A104 (= A108), F136 (= F140), H137 (= H141), D221 (= D226), V223 (= V228), Q224 (= Q229), K250 (= K255)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
42% identity, 97% coverage: 10:398/400 of query aligns to 5:384/390 of A0QYS9
- K304 (≠ E316) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
41% identity, 99% coverage: 3:397/400 of query aligns to 1:389/390 of 8ht4B
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
40% identity, 93% coverage: 16:386/400 of query aligns to 12:384/402 of 4jevB
- active site: F136 (= F140), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R374)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I50), S102 (= S106), G103 (= G107), T104 (≠ A108), F136 (= F140), H137 (= H141), E188 (= E193), E193 (= E198), D221 (= D226), V223 (= V228), Q224 (= Q229), K250 (= K255), R372 (= R374)
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 93% coverage: 16:386/400 of query aligns to 17:389/405 of P40732